ID A0A669CCV0_ORENI Unreviewed; 985 AA.
AC A0A669CCV0;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN Name=kdm4a {ECO:0000313|Ensembl:ENSONIP00000044711.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000044711.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000044711.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A669CCV0; -.
DR Ensembl; ENSONIT00000090859.1; ENSONIP00000044711.1; ENSONIG00000007297.2.
DR GeneTree; ENSGT00940000154930; -.
DR Proteomes; UP000005207; Linkage group LG15.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20463; Tudor_JMJD2A_rpt1; 1.
DR CDD; cd20466; Tudor_JMJD2A_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047479; Tudor_KDM4A_rpt1.
DR InterPro; IPR047481; Tudor_KDM4A_rpt2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF51; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 14..56
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 142..308
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 692..805
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 355..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 111245 MW; 84344FCBEC8F70C7 CRC64;
MTTDTPAQSV GCRVMTFTPS KEEFKDFGRY IAFMESQGAH RAGMAKVIPP KGWKPRKTYD
DIDDLVIPAP IQQVVTGQSG LFTQYNIQKK PMTVHDFRKT SNMDKFCSPR YVDFDELERK
FWKNLTFNPP LYGADVSGTL YDPDVTEWNI GHLNTILDIV ENESGIKIKG VNTPYLYFGM
WKSAFAWHTE DMDLYSINYL HFGEPKSWYV VPPEHGKRLE RLAKGFFPGN VQGCEAFLRH
KMTLISPFIL KKYGIPFEKV TQEAGQFIVT FPFGYHAGFN HGFNCAESTN FATQRWIDYG
KQATLCSCRQ DMVKISMDVF VRKFQPERYK LWKAGKDNAP IDHSKPTPEA AEFLKEDKKL
EPSKESPAEV PPEEPNTPVQ EDKRSGFISK SQSKANAKKT SNRRSPLKKE KNCVVAMDVS
ASEPTENQVV SLGAEETGGS EEPPLGNSCS KMFQRTLSPA DVLHVHSYAK GDYGDGEVLS
REEKKSEDSD HETEEDNSRV GKAVSGHIFN IVSYPFIDHS KCVVFAFCAS ETPEEPPPVE
AGGVEGEGWA KPLAHLWQSR PPNLKKEREY NQRIGSKPPY CSICLLFHTY HQVISGRADT
ECANSIDTHV MVAGERMRTK PLIPEMCFTT TTEDDAECEE QPVPPRLEED GTSLLISCSQ
CSVRVHASCY GVDPASVSKE WKCARCKANA MTENCCLCSL RGGALQKANN NKWVHVLCAV
AVLEARFVNI TERSPVDLSG IPLQRFKLKC YYCKKRMKKA SGCCVQCSHG RCPTAYHPTC
AQAAGVLMQP DEWPFVVHVT CCRHKGPAQI ERNKAAMHEL TVGQKVICKH KNGRYYQCDV
VQLSKETFYE VNFDDGSFSD NLFPEDIVSR DCAQLGPPPQ GEVVQVRWTD GLVYGAKFVA
AHVIQMYLVE FEDGSQLTAK RDDVYSLDEE LPKRVKTRLS KASDMRFDGI FEEKEIIQES
KRQRVINSRY RGDYIEPVIY RAIME
//
